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  • Articles: DFG German National Licenses  (4)
  • Pituitary  (2)
  • Rabbit  (2)
  • ACTH/MSH cells  (1)
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  • Articles: DFG German National Licenses  (4)
Material
Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Insulin inhibits lipolytic activity and degradation of β-lipotropin in rabbit adipose tissue
    Amsterdam : Elsevier
    Regulatory Peptides 29 (1990), S. 257-266 
    Details
    ISSN: 0167-0115
    Keywords: Adipose tissue ; Insulin ; Lipolytic activity ; Rabbit
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-0115(90)90088-E
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Evidence that lipolytic peptide B occurs in the ACTH/MSH-cells of the pituitary and in the brain (1980)
    Springer
    Cell & tissue research 205 (1980), S. 349-359 
    Details
    ISSN: 1432-0878
    Keywords: Lipolytic peptide B ; Pituitary ; ACTH/MSH cells ; Brain ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Several lipid-mobilizing peptides occur in the pituitary, among them β-lipotropin and “lipolytic peptide A and peptide B”. The latter two peptides are distinct from β-lipotropin and appear to be chemically related to the neurophysins. Immunohistochemistry has now revealed that the lipolytic peptide B of the pituitary is localized in the ACTH- and MSH-cells. In addition, immunoreactive peptide B was found in axons of the posterior lobe of the pituitary. Immunoreactive peptide B was found also in nerve fibers and nerve cell bodies in the hypothalamus, particularly in the hypothalamo-hypophyseal tract and in the magnocellular neuronal system. Immunoreactive nerve fibers were numerous also in the periventricular nucleus of the thalamus. The antiserum against peptide B cross-reacts with neurophysin I, and hence, it cannot be excluded that at least part of the immunostaining in the brain reflects the presence of the latter component. However, the regional distribution of immunoreactive peptide B and neurophysin was not identical. Therefore, it is possible that authentic peptide B occurs not only in the pituitary but also in the brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232277
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Untersuchungen über biologische Wirkungen eines lipolytisch wirksamen Peptids aus Schweinehypophysen (Fraktion H) (1969)
    Springer
    Clinical and experimental medicine 149 (1969), S. 139-144 
    Details
    ISSN: 1591-9528
    Keywords: Fraction H ; Enzymeactivities ; Liver ; Adipose ; Rabbit ; Fraktion H ; Enzymaktivitäten ; Leber ; Fettgewebe ; Kaninchen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung 2 Std nach Injektion von 500 μg Fraktion H wurden bei Kaninchen in Fettgewebe und Leber neun Schlüsselenzyme untersucht und mit den Befunden bei Kontrolltieren verglichen. Die signifikante Aktivitätsabnahme von Glucose-6-Phosphathehydrogenase (EC.1.1.1.49), Malatdehydrogenase (EC.1.1.1.37) und α-Glycerophosphatdehydrogenase (EC.1.1.1.8) im Fettgewebe wird mit einer herabgesetzten Triglyceridsynthese unter den Bedingungen der akuten Lipolyse in vivo erklärt. Hexokinase (EC.2.7.1.1), Phosphofructokinase (EC.2.7.1.11) und Pyruvatkinase (EC.2.7.1.40) als Schlüsselenzyme der Glycolyse waren im Fettgewebe nicht signifikant verändert. Neben den genannten Enzymen wurden in der Leber zum gleichen Zeitpunkt außerdem die Glycerokinase (EC.2.7.1.30), die Fructose-1,6-Diphosphatase (EC.3.1.3.11) und die Glucose-6-Phosphatase (EC.3.1.3.9) untersucht; keines der in der Leber bestimmten Enzyme zeigte eine signifikante Aktivitätsänderung.
    Notes: Summary Nine key enzymes in adipose tissue and liver of rabbits are investigated 2 hours after subcutanous injection of 500 μg Fraction H; the results are compared to those from normal animals. The activities of glucose-6-phosphate-dehydrogenase (EC.1.1.1.49), malatdehydrogenase (EC.1.1.1.37) and α-glycero-phosphate-dehydrogenase (EC.1.1.1.8) are diminished in adipose tissue suggesting a lowered glycerid-glycerolsynthesis under the conditions of acute lipolysis in vivo. Hexokinase (EC.2.71.1) phosphofructokinase (EC.2.7.1.11) and pyruvatkinase (EC.2.7.1.40) were not affected significantly in adipose tissue. Besides these enzymes glycerokinase (EC.2.7.1.30), fructose-1,6-diphosphatase (EC.3.1.3.11) and glucose-6-phosphatase (EC.3.1.3.9) were investigated in liver; no significant changes could be demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02044805
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Untersuchungen über eine lipolytisch wirksame Substanz aus Schweinehypophysen (Fraktion H) (1968)
    Springer
    Clinical and experimental medicine 147 (1968), S. 246-252 
    Details
    ISSN: 1591-9528
    Keywords: Lipolysis ; Fraction H ; Pituitary ; Purification ; Lipolyse ; Fraktion H ; Hypophyse ; Reinigung
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird über die Gewinnung und weitere säulenchromatographische Reinigung einer lipolytisch wirksamen Substanz aus Schweinehypophysen (Fraktion H) berichtet. Auf Grund der untersuchten physikalisch-chemischen Eigenschaften kann gesagt werden, daß diese Substanz mit der vonRudman et al. extrahierten Fraktion H identisch ist. Durch Chromatographie an Sephadex G 50 konnte die Fraktion weiter gereinigt werden; die lipolytische Aktivität pro Gewichtseinheit wurde dadurch von 0,3 Μg auf 0,1 Μg in vitro bzw. von 125 Μg auf 63 Μg in vivo als minimal wirksame Dosen gesteigert, wie Untersuchungen an Meerschweinchen und Kaninchen ergaben. Eine Kontamination mit lipolytisch wirksamen Mengen ACTH wurde durch säulenehromatographische Untersuchungen auf Sephadex G 50 weitgehend ausgeschlossen.
    Notes: Summary The extraction and further purification of a lipolytic substance from hog pituitaries (Fraction H) are reported. This substance has physico-chemical properties identical with Fraction H extracted from pituitaries of pigs byRudman et al. Further purification was achieved by Sephadex-chromatographie. The lipolytic activity in the rabbit was augmented in vitro to 0.1 Μg/ml and in vivo to 63 Μg as minimal effective dose. A contamination with ACTH could be excluded by chromatography on Sephadex G 50.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02044608
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    Paper (German National Licenses)
    Fulltext
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